END8_KLEP3
ID END8_KLEP3 Reviewed; 263 AA.
AC B5XZD9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Endonuclease 8 {ECO:0000255|HAMAP-Rule:MF_01253};
DE AltName: Full=DNA glycosylase/AP lyase Nei {ECO:0000255|HAMAP-Rule:MF_01253};
DE EC=3.2.2.- {ECO:0000255|HAMAP-Rule:MF_01253};
DE EC=4.2.99.18 {ECO:0000255|HAMAP-Rule:MF_01253};
DE AltName: Full=DNA-(apurinic or apyrimidinic site) lyase Nei {ECO:0000255|HAMAP-Rule:MF_01253};
DE AltName: Full=Endonuclease VIII {ECO:0000255|HAMAP-Rule:MF_01253};
GN Name=nei {ECO:0000255|HAMAP-Rule:MF_01253}; OrderedLocusNames=KPK_3844;
OS Klebsiella pneumoniae (strain 342).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=507522;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=342;
RX PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W.,
RA Methe B.A.;
RT "Complete genome sequence of the N2-fixing broad host range endophyte
RT Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL PLoS Genet. 4:E1000141-E1000141(2008).
CC -!- FUNCTION: Involved in base excision repair of DNA damaged by oxidation
CC or by mutagenic agents. Acts as DNA glycosylase that recognizes and
CC removes damaged bases. Has a preference for oxidized pyrimidines, such
CC as thymine glycol, 5,6-dihydrouracil and 5,6-dihydrothymine. Has AP
CC (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA
CC strand. Cleaves the DNA backbone by beta-delta elimination to generate
CC a single-strand break at the site of the removed base with both 3'- and
CC 5'-phosphates. {ECO:0000255|HAMAP-Rule:MF_01253}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-
CC deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-
CC dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-
CC 2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-
CC COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695,
CC ChEBI:CHEBI:167181; EC=4.2.99.18; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01253};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01253};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01253};
CC -!- SIMILARITY: Belongs to the FPG family. {ECO:0000255|HAMAP-
CC Rule:MF_01253}.
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DR EMBL; CP000964; ACI06680.1; -; Genomic_DNA.
DR AlphaFoldDB; B5XZD9; -.
DR SMR; B5XZD9; -.
DR EnsemblBacteria; ACI06680; ACI06680; KPK_3844.
DR KEGG; kpe:KPK_3844; -.
DR HOGENOM; CLU_038423_2_2_6; -.
DR OMA; TYWCPRC; -.
DR OrthoDB; 1162346at2; -.
DR Proteomes; UP000001734; Chromosome.
DR GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0000703; F:oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR CDD; cd08965; EcNei-like_N; 1.
DR Gene3D; 3.20.190.10; -; 1.
DR HAMAP; MF_01253; Endonuclease_8; 1.
DR InterPro; IPR015886; DNA_glyclase/AP_lyase_DNA-bd.
DR InterPro; IPR015887; DNA_glyclase_Znf_dom_DNA_BS.
DR InterPro; IPR044091; EcNei-like_N.
DR InterPro; IPR023713; Endonuclease-VIII.
DR InterPro; IPR012319; FPG_cat.
DR InterPro; IPR035937; MutM-like_N-ter.
DR InterPro; IPR010979; Ribosomal_S13-like_H2TH.
DR InterPro; IPR000214; Znf_DNA_glyclase/AP_lyase.
DR InterPro; IPR010663; Znf_FPG/IleRS.
DR Pfam; PF01149; Fapy_DNA_glyco; 1.
DR Pfam; PF06831; H2TH; 1.
DR Pfam; PF06827; zf-FPG_IleRS; 1.
DR SMART; SM00898; Fapy_DNA_glyco; 1.
DR SMART; SM01232; H2TH; 1.
DR SUPFAM; SSF46946; SSF46946; 1.
DR SUPFAM; SSF81624; SSF81624; 1.
DR PROSITE; PS51068; FPG_CAT; 1.
DR PROSITE; PS01242; ZF_FPG_1; 1.
DR PROSITE; PS51066; ZF_FPG_2; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA repair; DNA-binding; Glycosidase; Hydrolase; Lyase;
KW Metal-binding; Multifunctional enzyme; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01253"
FT CHAIN 2..263
FT /note="Endonuclease 8"
FT /id="PRO_1000139938"
FT ZN_FING 229..263
FT /note="FPG-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01253"
FT ACT_SITE 2
FT /note="Schiff-base intermediate with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01253"
FT ACT_SITE 3
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01253"
FT ACT_SITE 53
FT /note="Proton donor; for beta-elimination activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01253"
FT ACT_SITE 253
FT /note="Proton donor; for delta-elimination activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01253"
FT BINDING 70
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01253"
FT BINDING 125
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01253"
FT BINDING 169
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01253"
SQ SEQUENCE 263 AA; 29514 MW; 675B11290662E9F5 CRC64;
MPEGPEIRRA ADKLEAAIKG EPLTDAWFAF PQLQPYQSLL IGQRVTHIAT RGKALLTHFS
GGLTLYSHNQ LYGVWRVVDA GEQPASNRVL RVRLQTARKA ILLYSASDIE MLTAEQVAHH
PFLLRVGPDV LDMTLTVEEV KARLLSAKFR HRQFSGLLLD QAFLAGLGNY LRVEILWQVG
LSGKRKAAEL SDSQLDALAH ALLAIPRLSY HTRGQADDNK HHGALFRFKV FHRDGERCER
CGGVIEKTTL SSRPFYWCPG CQH
